DHX15_SCHPO
ID DHX15_SCHPO Reviewed; 735 AA.
AC O42945; Q9USE5;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Probable pre-mRNA-splicing factor ATP-dependent RNA helicase prp43;
DE EC=3.6.4.13;
GN Name=prp43; ORFNames=SPBC16H5.10c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 536-729, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Pre-mRNA processing factor involved in disassembly of
CC spliceosomes after the release of mature mRNA. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10759889,
CC ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC DDX15/PRP43 sub-subfamily. {ECO:0000305}.
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DR EMBL; CU329671; CAA17908.1; -; Genomic_DNA.
DR EMBL; AB027819; BAA87123.1; -; Genomic_DNA.
DR PIR; T39615; T39615.
DR RefSeq; NP_595937.1; NM_001021845.2.
DR AlphaFoldDB; O42945; -.
DR SMR; O42945; -.
DR BioGRID; 276595; 40.
DR IntAct; O42945; 3.
DR STRING; 4896.SPBC16H5.10c.1; -.
DR iPTMnet; O42945; -.
DR MaxQB; O42945; -.
DR PaxDb; O42945; -.
DR EnsemblFungi; SPBC16H5.10c.1; SPBC16H5.10c.1:pep; SPBC16H5.10c.
DR GeneID; 2540057; -.
DR KEGG; spo:SPBC16H5.10c; -.
DR PomBase; SPBC16H5.10c; prp43.
DR VEuPathDB; FungiDB:SPBC16H5.10c; -.
DR eggNOG; KOG0925; Eukaryota.
DR HOGENOM; CLU_001832_5_11_1; -.
DR InParanoid; O42945; -.
DR OMA; DHDLKRY; -.
DR PhylomeDB; O42945; -.
DR PRO; PR:O42945; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0071014; C:post-mRNA release spliceosomal complex; IDA:PomBase.
DR GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR GO; GO:0005684; C:U2-type spliceosomal complex; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; ISS:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; ISS:UniProtKB.
DR GO; GO:0000390; P:spliceosomal complex disassembly; IPI:PomBase.
DR CDD; cd17973; DEXHc_DHX15; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR044756; DHX15_DEXHc.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF04408; HA2; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding; Helicase; Hydrolase; mRNA processing; mRNA splicing;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..735
FT /note="Probable pre-mRNA-splicing factor ATP-dependent RNA
FT helicase prp43"
FT /id="PRO_0000055144"
FT DOMAIN 85..250
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 275..455
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 197..200
FT /note="DEAH box"
FT COMPBIAS 15..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 98..105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 735 AA; 83804 MW; DC2A25F145F5A5C4 CRC64;
MEPAQKKLRQ ESKNPYLAHL NNGDDSEEVV SSKGLTRRAT TVAQAAKAEE GPNNFFNDKP
FSQNYFKILE TRRELPVYQQ REEFLKIYHE NQIIVFVGET GSGKTTQIPQ FVLYDELPHL
TNTQIACTQP RRVAAMSVAK RVADEMDVDL GEEVGYNIRF EDCSGPNTLL KYMTDGMLLR
EAMTDHMLSR YSCIILDEAH ERTLATDILM GLMKRLATRR PDLKIIVMSA TLDAKKFQKY
FFDAPLLAVP GRTYPVEIYY TQEPERDYLE AALRTVLQIH VEEGPGDILV FLTGEEEIED
ACRKITLEAD DLVREGAAGP LKVYPLYGSL PPNQQQRIFE PTPEDTKSGY GRKVVISTNI
AETSLTIDGI VYVVDPGFSK QKIYNPRIRV ESLLVSPISK ASAQQRAGRA GRTRPGKCFR
LYTEEAFRKE LIEQTYPEIL RSNLSSTVLE LKKLGIDDLV HFDYMDPPAP ETMMRALEEL
NYLNCLDDNG DLTPLGRKAS EFPLDPNLAV MLIRSPEFYC SNEVLSLTAL LSVPNVFVRP
NSARKLADEM RQQFTHPDGD HLTLLNVYHA YKSGEGTADW CWNHFLSHRA LISADNVRKQ
LRRTMERQEV ELISTPFDDK NYYVNIRRAL VSGFFMQVAK KSANGKNYVT MKDNQVVSLH
PSCGLSVTPE WVVYNEFVLT TKSFIRNVTA IRPEWLIELA PNYYDLDDFD NNKEVKSALQ
KVYQMAARSK KNARR
